Determination of the Molecular Weights of Uroprotein Fractions with Urokinase Activity by Means of Molecular Sieving

Doleschel, W; Auerswald, W

doi:10.1159/000136994

Cited by 7 publications

(4 citation statements)

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“…They found a molecular weight of 34,500 and reported an active contaminant with a molecular weight above 100,000. Doleschel and Auerswald (1967) studied a concentrate from normal urine by gel filtration at pH 8.2 in 0.1 m Tris buffer with 1 m NaCl. They observed a wide distribution of activator activity over fractions of different sizes except the smallest.…”

Section: Discussionmentioning

confidence: 99%

Isolation and purification of a tissue plasminogen activator and its comparison with urokinase

Kok¹,

Astrup²

1969

Biochemistry

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Section: Discussionmentioning

confidence: 99%

Isolation and purification of a tissue plasminogen activator and its comparison with urokinase

Kok¹,

Astrup²

1969

Biochemistry

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“…When the urokinase activities are correlated with the molecular classes, which --as we have demonstrated (Doleschel and Auerswald, 1967) --represent the urokinase monomer, dimer, and polymer, it becomes obvious that the urokinase monomer predominates in neonates with about 70% of the total urokinase activity, while in infants and adults it represents 40 and 30% respectively of the total activity. On the other hand, the uroldnase dimer and polymer play only a minor role in the urine of neonates as compared with the other 2 groups.…”

Section: Discussion Of Resultsmentioning

confidence: 61%

“…In our investigation of uroproteins (Doleschel and Auerswald, 1967) it was our aim to apply fractionation procedures permitting exact classification according to molecular weights, especially in the lower range. By means of molecular sieving with Sephadex G-150, we sueeeeded in classifying the uroprotein spectrum of the adult according to molecular weight; we found, furthermore, that urokinase is present in the urine in several forms; as a monomer, and in various degrees of polymerization.…”

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confidence: 99%

Uroprotein excretion in neonates and infants

1971

Self Cite

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Abstraot. In 5 neonates and 5 infants urinary proteins were investigated for quantity, molecular weight and fibrinolytic activity, the urine of 5 adults serving as a control. The uroproteins were concentrated and fractionated by means of molecular sieving . Urokinase activities were determined on native human fibrin plates.1. The distribution of the uroproteins among the various molecular classes showed no difference between age groups.2. In all age groups urokinase activities were present in the ranges of molecular weights 30000, 60000 and above 100000, representing the monomer, dimer and polymer forms of urokinase.3. There is a significant difference between the distribution of the urokinase activities over the molecular weight ranges in the different age groups. In neonates 70% of the urokinase is present as monomer, 25% as dimer and 5% as polymer, while in infants and adults the urokinase is present in about equal parts as mono-, di-and polymer.The possible importance is discussed of the finding that, as the organism matures, there is a decreasing tendency for urokinase to pass fluid compartment barriers.

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“…In the present experiments it was only important to establish two density-gradient profiles, one for radioactivity of the 131 I-labeled clinical product and the other for urokinase activity (Fig.3). Because three different molecular weights ranging from 31,500 to 54,000 to 104,000 have been reported for urokinase (18,24,30), the spread of activity over the entire range of the second peak was not unexpected. The first peak was clearly the non-dialyzable, nonantigenic and non-enzymatic portion of the radioiodinated clinical preparation.…”

Section: Density-gradient Ultracentrifugation Of Radioiodinated Urokimentioning

confidence: 91%

Plasminogen-Fibrinogen Complex Formation as a Prelude to Fibrinogenolysis

Ball¹,

Silver²,

Day³

1971

Thromb Haemost

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SummaryReproducible density-gradient ultracentrifugation reference profiles of the ratezonal type were established individually for radioiodinated fibrinogen, plasminogen, and urokinase. Two- and three-component radioiodinated mixtures were then studied to determine whether stable complexes would form between any two components and thus change the density-gradient distribution profiles.Urokinase did not form stable complexes with plasminogen, fibrinogen, or fibrin, nor with any plasminogen-fibrinogen or plasminogen-fibrin mixtures.Plasminogen was found to form stable complexes with fibrinogen and with fibrin. Urokinase added to such mixtures resulted in fibrinogenolysis and fibrinolysis, but not in stable urokinase binding.The data support the proposition that urokinase does not activate plasminogen directly but requires the formation of plasminogen-fibrin(ogen) complexes as a prelude (conformational change?) to plasmin conversion and subsequent fibrin(ogen)olysis.

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Determination of the Molecular Weights of Uroprotein Fractions with Urokinase Activity by Means of Molecular Sieving

Cited by 7 publications

References 1 publication

Isolation and purification of a tissue plasminogen activator and its comparison with urokinase

Isolation and purification of a tissue plasminogen activator and its comparison with urokinase

Uroprotein excretion in neonates and infants

Plasminogen-Fibrinogen Complex Formation as a Prelude to Fibrinogenolysis

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